Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An inhibitor of papain and other SH-proteases was purified 520-fold from human epidermis extracts by acetone fractionation, heat treatment, papain-Sepharose affinity chromatography, and Sephadex G-50 chromatography. The purified inhibitor had a molecular weight of 12,600 and contained no hexose, as tested by the anthrone reaction. The inhibitor survived in a boiling water bath, in 5% trichloroacetic acid, 20 mM Na3PO4 (pH 12.1) and 4 M NH4OH (pH 11.9). By isoelectric focusing 2 major activity peaks with pI's of 4.6 and 4.8, and a minor peak with a pI of 4.9 was fractioned, and 3 corresponding protein bands were seen after analytical isoelectric focusing. Immunization of rabbits with the purified inhibitor yielded a highly specific anti-inhibitor serum. The purified inhibitor inhibited papain, ficin, human cathepsins B and C, and slightly inhibited bromelain. No inhibition of serine proteases (bovine trypsin and chymotrypsin A, porcine elastase) or an acid protease (human cathepsin D) was observed. Evidence was obtained that the inhibitor formed a complex with both dithiothreitol-activated papain and enzymatically inactive mercuripapain.
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PMID:Purification and some characteristics of the human epidermal SH-protease inhibitor. 68 77

It has been shown that low concentrations of E. coli lipopolysaccharides (LPS) greatly and selectively stimulate phagocytosis and related functions in mouse bone marrow-derived macrophages. Culture in the presence of 50 ng/ml LPS induced on average a 10-fold enhancement of phagocytosis of IgG-coated sheep erythrocytes. Activation was in two stages--a small increase observed during the first 8 to 12 hr, and the major increase noted between 16 and 24 hr. Phagocytic activity remained at the maximal level for 24 hr and then declined progressively. Stimulation by LPS was dose-dependent; significant effects could be observed at 0.8 ng/ml and the maximum was reached at 10 ng/ml. LPS-treated cells also showed a markedly increased tendency to form colonies. All these effects could be prevented by the addition of 100 ng/ml polymyxin B together with LPS, indicating that the active principle is lipid A. The LPS-dependent increase in phagocytic activity is probably mediated by increased Fc receptor capacity because both parameters were influenced in parallel by the stimulus. Phagocytosis-related events, such as enhanced hexose monophosphate shunt activity, H2O2 formation, and nitroblue tetrazolium reduction were also stimulated by LPS. By contrast, pinocytosis was unaffected. Measurements of cell-associated enzyme activities showed that lactate dehydrogenase, acid phosphatase, and cathepsin D were significantly increased. Beta-glucuronidase, beta-galactosidase, alkaline phosphodiesterase, and aminopeptidase were unchanged and NAD nucleosidase was markedly decreased after LPS treatment. 5'-Nucleotidase and glucosamine uptake were undetectable both in control and LPS-stimulated cells. LPS treatment induced a significant increase in cell-associated protein, but did not result in cell proliferation or increased cell loss as shown by the DNA content that remained constant. LPS-induced changes were dependent on de novo protein synthesis; cycloheximide prevented enhancement of phagocytosis, Fc receptor capacity, and colony formation.
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PMID:Stimulation of phagocytosis in bone marrow-derived mouse macrophages by bacterial lipopolysaccharide: correlation with biochemical and functional parameters. 673 51

Adjuvant induced arthritis in rats was studied by the changes in serum and urinary protein-bound carbohydrate metabolites, changes in serum and tissue lysosomal glycohydrolases and lysosomal fragility. From the second week onwards the urinary excretion of hexosamine and uronic acid is increased. Serum levels of protein bound hexose, hexosamine, sialic acid and fucose are increased significantly in both the acute and chronic phases of the disease. There is no change in the total activity of lysosomal glycohydrolases, viz., beta-glucuronidase, beta-N-acetyl glucosaminidase and cathepsin D in the tissues of liver, kidney and spleen except that of liver enzymes in the chronic phase which are elevated significantly. The free activities of lysosomal glycohydrolases investigated, viz., beta-glucuronidase, beta-N-acetyl glucosaminidase, beta-galactosidase, alpha-mannosidase and cathepsin D are increased in liver and spleen in the acute phase. The free activities of beta-glucuronidase, beta-N-acetyl glucosaminidase and cathepsin D of kidney showed no change whereas those of beta-galactosidase and alpha-mannosidase are increased. In the chronic phase of the disease the free activities of all glycohydrolases are significantly increased in all tissues. Serum glycohydrolases are significantly increased in both acute and chronic phases. Studies on lysosomal preparations showed increased fragility of lysosomes derived from liver and kidney of arthritic rats in both phases of the disease.
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PMID:Glycohydrolases and lysosomal stability in adjuvant induced arthritis. 738 Jun 46